Abstract
An orange-coloured protein (ORP) isolated from Desulfovibrio gigas, a sulphate reducer, has been previously shown by extended X-ray absorption fine structure (EXAFS) to contain a novel mixed-metal sulphide cluster of the type [S2MoS2CuS2MoS2] [J. Am. Chem. Soc. 122 (2000) 8321]. We report here the purification and the biochemical/ spectroscopic characterisation of this novel protein. ORP is a soluble monomeric protein (11.8 kDa). The cluster is non-covalently bound to the polypeptide chain. The presence of a MoS4 2- moiety in the structure of the cofactor contributes with a quite characteristic UV-Vis spectra, exhibiting an orange colour, with intense absorption peaks at 480 and 338 nm. Pure ORP reveals an Abs480/Abs338 ratio of 0.535. The gene sequence coding for ORP as well as the amino acid sequence was determined. The putative biological function of ORP is discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 833-840 |
| Number of pages | 8 |
| Journal | Journal of Inorganic Biochemistry |
| Volume | 98 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 1 Jan 2004 |
Keywords
- Copper
- Desulfovibrio gigas
- Heterometallic cluster
- Molybdenum
- Tetrathiomolybdate
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